ID   C94A2_VICSA             Reviewed;         513 AA.
AC   P98188;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytochrome P450 94A2;
DE            EC=1.14.-.-;
DE   AltName: Full=P450-dependent fatty acid omega-hydroxylase;
GN   Name=CYP94A2; Synonyms=VAGH811;
OS   Vicia sativa (Spring vetch) (Tare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seedling;
RX   PubMed=10405339; DOI=10.1006/bbrc.1999.0999;
RA   Le Bouquin R., Pinot F., Benveniste I., Salauen J.-P., Durst F.;
RT   "Cloning and functional characterization of CYP94A2, a medium chain fatty
RT   acid hydroxylase from Vicia sativa.";
RL   Biochem. Biophys. Res. Commun. 261:156-162(1999).
CC   -!- FUNCTION: Catalyzes the omega-hydroxylation of various fatty acids
CC       (FA). The substrate specificity is higher for myristate > laurate =
CC       palmitate (C14>C16=C12).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Weakly expressed in seedlings.
CC   -!- INDUCTION: By clofibrate; weakly.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF092917; AAG33645.1; -; mRNA.
DR   AlphaFoldDB; P98188; -.
DR   SMR; P98188; -.
DR   PRIDE; P98188; -.
DR   KEGG; ag:AAG33645; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..513
FT                   /note="Cytochrome P450 94A2"
FT                   /id="PRO_0000052193"
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         455
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   513 AA;  58419 MW;  BEA213B45837B1A7 CRC64;
     MELETLISWL LFSTSLFWFL FLATKTKSKP PKTPSSTTNT PIPKSYPIFG SAFSLLANFH
     RRIQWTSDIL QTIPSSTFVL HRPFGARQVF TAQPAVVQHI LRTNFTCYGK GLTFYQSIND
     FLGDGIFNAD GESWKFQRQI SSHEFNTRSL RKFVETVVDV ELSDRLVPVL SQASNSQTTL
     DFQDILQRLT FDNICMIAFG YDPEYLLPSL PEIPFAKAFD ESSQLSIERL NALIPLLWKV
     KRFLNIGVER QLKEAVAEVR GLATKIVKNK KKELKEKALQ SESESVDLLS RFLSSGHSDE
     SFVTDMVISI ILAGRDTTSA ALTWFFWLLS KHSHVENEIL KEITGKSETV GYDEVKDMVY
     THAALCESMR LYPPLPVDTK VAVHDDVLPD GTLVKKGWRV TYHIYAMGRS EKIWGPDWAE
     FRPERWLSRD EVGKWSFVGI DYYSYPVFQA GPRVCIGKEM AFLQMKRVVA GIMGRFRVVP
     AMVEGIEPEY TAHFTSVMKG GFPVKIEKRS PLV